ID   AROH_ENTAG              Reviewed;         348 AA.
AC   O54459;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN   Name=aroH;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9422601; DOI=10.1128/jb.180.1.119-127.1998;
RA   Subramaniam P.S., Xie G., Xia T., Jensen R.A.;
RT   "Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase
RT   from Neisseria gonorrhoeae in the context of its membership in a protein
RT   family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate
RT   synthases.";
RL   J. Bacteriol. 180:119-127(1998).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC         phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC         Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; U93355; AAB96400.1; -; Genomic_DNA.
DR   AlphaFoldDB; O54459; -.
DR   SMR; O54459; -.
DR   STRING; 549.BW31_01626; -.
DR   eggNOG; COG0722; Bacteria.
DR   UniPathway; UPA00053; UER00084.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Transferase.
FT   CHAIN           1..348
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-
FT                   sensitive"
FT                   /id="PRO_0000140843"
SQ   SEQUENCE   348 AA;  37744 MW;  1673534B92523B76 CRC64;
     MNKTDELRTA RIGSLITPPS LAAEHPVSPA IADNVTAARK RIACILTGED HRLLVVIGPC
     SLHDPKAALE YAERLNALRR RYEDRLEIVM RAYFEKPRTV VGWKGLISDP DLDGSYDVNR
     GIGIARQLLI DINALGLPTA TEFLDMVIGQ FIADLISWGA IGARTTESQI HREMASALSC
     PVGFKNGTDG NVQIAVDAIR AARASHMFLS PDKLGQMTIY QTSGNPHGHV ILRGGKQPNY
     HASDVAAAAE SLSAFNLPQQ LVIDFSHGNC LKQHRRQMDV AAEVAEQIKA GSQAVAGVMI
     ESFLEEGNQK VVSGEPLVYG KSITDPCLGW QESEKVLALL AEAVSHRL